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Key Documents

ABF1070

Sigma-Aldrich

Anti-DRBP76/ILF3 Antibody

serum, from rabbit

同義詞:

Interleukin enhancer-binding factor 3, Double-stranded RNA-binding protein 76, DRBP76, M-phase phosphoprotein 4, MPP4, Nuclear factor associated with dsRNA, NFAR, Nuclear factor of activated T-cells 90 kDa, NF-AT-90, Translational control protein 80, TCP

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About This Item

分類程式碼代碼:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物源

rabbit

品質等級

抗體表格

serum

抗體產品種類

primary antibodies

無性繁殖

polyclonal

物種活性

human

技術

western blot: suitable

NCBI登錄號

UniProt登錄號

運輸包裝

dry ice

目標翻譯後修改

unmodified

基因資訊

human ... ILF3(3609)

一般說明

Interleukin enhancer-binding factor 3 (UniProt Q12906; also known as Double-stranded RNA-binding protein 76, DRBP76, dsRNA binding protein NFAR-2/MPP4, Interleukin enhancer binding factor 3 90kD, M-phase phosphoprotein 4, MPP4, NF-AT-90, NFAR, Nuclear factor associated with dsRNA, Nuclear factor of activated T-cells 90 kDa, TCP80, Translational control protein 80) is encoded by the ILF3 (also known as DRBF, NF90, MPHOSPH4) gene (Gene ID 3609) in human. DRBP76 is a dsRNA binding protein (DRBP) family member capable of binding both dsRNAs and highly structured single-stranded RNA molecules through its C-terminal region. DRBP76 influences the nucleus-cytoplasm export, stability, and translation of target mRNAs via direct interaction with their 3′ UTRs. DRBP76 is also reported to play both positive and negative regulatory roles in viral replications. DRBP76 is shown to interact with the 3′-terminal stem loop (SL) structure of the single-stranded RNA genome of the dengue virus and DRBP76 knockdown decreases production of functional dengue virus in cultured cells. On the other hand, DRBP76 can interact with full-length Zaire Ebola virus (EBOV) protein VP35 in the absence of exogenous dsRNA. Viral VP35 expression redistributes DRBP76 from the nucleus to the cytoplasm in the host cells and over-expression of DRBP76 impairs the function of the EBOV transcription/replication complex.

特異性

Expected to react with all 7 spliced isoforms.

免疫原

His-tagged recombinant protein corresponding to human DRBP76/ILF3.

應用

This Anti-DRBP76/ILF3 Antibody is validated for use in Western Blotting for the detection of DRBP76/ILF3.
Western Blotting Analysis: A representative lot detected DRBP76/ILF3 in the nuclear fractions prepared from the squamous cell carcinoma of the head and neck (SCCHN) cell lines PCI-15A and PCI-15B (Umemura, N., et al, (2012). Cancer Res. 72(1):45-55).
Western Blotting Analysis: A representative lot detected DRBP76/ILF3 in the nuclear fractions prepared from Wt11 (HEK293 expressing Flag-tagged wild-type TLR3) cells (Zhu, J., et al, (2010). J Immunol. 184(10):5768-5776; Sarkar, S.N., et al, (2004). Nat Struct Mol Biol. 11(11):1060-1067).

品質

Evaluated by Western Blotting in MDA-MB-435 cell lysate.

Western Blotting Analysis: A 1:500 of this antibody detected DRBP76/ILF3 in 10 µg of MDA-MB-435 cell lysate.

標靶描述

~100 kDa A lower size band ~75 kDa may be seen in some lysates, most likely representing a smaller size variant or a non-specific band. Uncharacterized band(s) may appear in some lysates.

其他說明

Concentration: Please refer to lot specific datasheet.

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儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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存取文件庫

Defective NF-?B signaling in metastatic head and neck cancer cells leads to enhanced apoptosis by double-stranded RNA.
Umemura, N; Zhu, J; Mburu, YK; Forero, A; Hsieh, PN; Muthuswamy, R; Kalinski, P; Ferris et al.
Cancer Research null
Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling.
Sarkar, SN; Peters, KL; Elco, CP; Sakamoto, S; Pal, S; Sen, GC
Nature Structural and Molecular Biology null
High-throughput screening for TLR3-IFN regulatory factor 3 signaling pathway modulators identifies several antipsychotic drugs as TLR inhibitors.
Zhu, J; Smith, K; Hsieh, PN; Mburu, YK; Chattopadhyay, S; Sen, GC; Sarkar, SN
Journal of immunology (Baltimore, Md. : 1950) (1950)
Jennifer L Martindale et al.
Bio-protocol, 10(2), e3488-e3488 (2020-01-20)
RNAs and RNA-binding proteins (RBPs) can interact dynamically in ribonucleoprotein (RNP) complexes that play important roles in controlling gene expression programs. One of the powerful ways to investigate changes in the association of RNAs with an RBP of interest is

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